GenomeNet

Database: UniProt
Entry: Q01543
LinkDB: Q01543
Original site: Q01543 
ID   FLI1_HUMAN              Reviewed;         452 AA.
AC   Q01543; B2R8H2; B4DFV4; B4DTC6; G3V183; Q14319; Q92480; Q9UE07;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   07-OCT-2020, entry version 217.
DE   RecName: Full=Friend leukemia integration 1 transcription factor;
DE   AltName: Full=Proto-oncogene Fli-1;
DE   AltName: Full=Transcription factor ERGB;
GN   Name=FLI1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHROMOSOMAL TRANSLOCATION.
RC   TISSUE=Bone marrow;
RX   PubMed=1522903; DOI=10.1038/359162a0;
RA   Delattre O., Zucman J., Plougastel B., Desmaze C., Melot T., Peter M.,
RA   Kovar H., Joubert I., de Jong P., Rouleau G., Aurias A., Thomas G.;
RT   "Gene fusion with an ETS DNA-binding domain caused by chromosome
RT   translocation in human tumours.";
RL   Nature 359:162-165(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=1445800;
RA   Watson D.K., Smyth F.E., Thompson D.M., Cheng J.Q., Testa J.R., Papas T.S.,
RA   Seth A.;
RT   "The ERGB/Fli-1 gene: isolation and characterization of a new member of the
RT   family of human ETS transcription factors.";
RL   Cell Growth Differ. 3:705-713(1992).
RN   [3]
RP   SEQUENCE REVISION.
RA   Watson D.;
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=1394211;
RA   Prasad D.D., Rao V.N., Reddy E.S.;
RT   "Structure and expression of human Fli-1 gene.";
RL   Cancer Res. 52:5833-5837(1992).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Blood;
RX   PubMed=8439553; DOI=10.1016/0167-4781(93)90283-j;
RA   Hromas R., May W., Denny C., Raskind W., Moore J., Maki R.A., Beck E.,
RA   Klemsz M.J.;
RT   "Human FLI-1 localizes to chromosome 11q24 and has an aberrant transcript
RT   in neuroepithelioma.";
RL   Biochim. Biophys. Acta 1172:155-158(1993).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND CHROMOSOMAL
RP   TRANSLOCATION.
RX   PubMed=1765382; DOI=10.1016/0888-7543(91)90124-w;
RA   Baud V., Lipinski M., Rassart E., Poliquin L., Bergeron D.;
RT   "The human homolog of the mouse common viral integration region, FLI1, maps
RT   to 11q23-q24.";
RL   Genomics 11:223-224(1991).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Ubhi B.T.S., Rainey D.R., Meredith D.M.;
RL   Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC   TISSUE=Amygdala, Placenta, and Thymus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lymph;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 58-452.
RX   PubMed=9751743; DOI=10.1073/pnas.95.20.11786;
RA   Zucman-Rossi J., Legoix P., Victor J.M., Lopez B., Thomas G.;
RT   "Chromosome translocation based on illegitimate recombination in human
RT   tumors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:11786-11791(1998).
RN   [13]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 278-301.
RC   TISSUE=Placenta;
RX   PubMed=7542907; DOI=10.1002/gcc.2870130209;
RA   Bhagirath T., Abe S., Nojima T., Yoshida M.C.;
RT   "Molecular analysis of a t(11;22) translocation junction in a case of
RT   Ewing's sarcoma.";
RL   Genes Chromosomes Cancer 13:126-132(1995).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [15]
RP   FUNCTION, INVOLVEMENT IN BDPLT21, VARIANTS BDPLT21 TRP-337 AND CYS-343, AND
RP   CHARACTERIZATION OF VARIANTS BDPLT21 TRP-337 AND CYS-343.
RX   PubMed=24100448; DOI=10.1182/blood-2013-06-506873;
RG   UK Genotyping and Phenotyping of Platelets Study Group;
RA   Stockley J., Morgan N.V., Bem D., Lowe G.C., Lordkipanidze M., Dawood B.,
RA   Simpson M.A., Macfarlane K., Horner K., Leo V.C., Talks K., Motwani J.,
RA   Wilde J.T., Collins P.W., Makris M., Watson S.P., Daly M.E.;
RT   "Enrichment of FLI1 and RUNX1 mutations in families with excessive bleeding
RT   and platelet dense granule secretion defects.";
RL   Blood 122:4090-4093(2013).
RN   [16]
RP   FUNCTION, INVOLVEMENT IN BDPLT21, VARIANT BDPLT21 TRP-324, AND
RP   CHARACTERIZATION OF VARIANT BDPLT21 TRP-324.
RX   PubMed=26316623; DOI=10.1182/blood-2015-06-650887;
RA   Stevenson W.S., Rabbolini D.J., Beutler L., Chen Q., Gabrielli S.,
RA   Mackay J.P., Brighton T.A., Ward C.M., Morel-Kopp M.C.;
RT   "Paris-Trousseau thrombocytopenia is phenocopied by the autosomal recessive
RT   inheritance of a DNA-binding domain mutation in FLI1.";
RL   Blood 126:2027-2030(2015).
RN   [17]
RP   FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN BDPLT21, VARIANTS BDPLT21
RP   GLN-337 AND GLU-345, AND CHARACTERIZATION OF VARIANTS BDPLT21 GLN-337 AND
RP   GLU-345.
RX   PubMed=28255014; DOI=10.3324/haematol.2016.153577;
RA   Saultier P., Vidal L., Canault M., Bernot D., Falaise C., Pouymayou C.,
RA   Bordet J.C., Saut N., Rostan A., Baccini V., Peiretti F., Favier M.,
RA   Lucca P., Deleuze J.F., Olaso R., Boland A., Morange P.E., Gachet C.,
RA   Malergue F., Faure S., Eckly A., Tregouet D.A., Poggi M., Alessi M.C.;
RT   "Macrothrombocytopenia and dense granule deficiency associated with FLI1
RT   variants: ultrastructural and pathogenic features.";
RL   Haematologica 102:1006-1016(2017).
RN   [18]
RP   STRUCTURE BY NMR OF 276-373.
RX   PubMed=7773776; DOI=10.1038/nsb1294-871;
RA   Liang H., Mao X., Olejniczak E.T., Nettesheim D.G., Yu L., Meadows R.P.,
RA   Thompson C.B., Fesik S.W.;
RT   "Solution structure of the ets domain of Fli-1 when bound to DNA.";
RL   Nat. Struct. Biol. 1:871-875(1994).
RN   [19]
RP   STRUCTURE BY NMR OF 114-198.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the SAM_pnt-domain of the human Friend leukemia
RT   integration 1 transcription factor.";
RL   Submitted (NOV-2005) to the PDB data bank.
CC   -!- FUNCTION: Sequence-specific transcriptional activator (PubMed:24100448,
CC       PubMed:26316623, PubMed:28255014). Recognizes the DNA sequence 5'-
CC       C[CA]GGAAGT-3'. {ECO:0000269|PubMed:24100448,
CC       ECO:0000269|PubMed:26316623, ECO:0000269|PubMed:28255014}.
CC   -!- SUBUNIT: Can form homodimers or heterodimers with ETV6/TEL1.
CC   -!- INTERACTION:
CC       Q01543; P56545-3: CTBP2; NbExp=3; IntAct=EBI-2271018, EBI-10171902;
CC       Q01543; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-2271018, EBI-747107;
CC       Q01543; O94993: SOX30; NbExp=3; IntAct=EBI-2271018, EBI-742973;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28255014}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q01543-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q01543-2; Sequence=VSP_001478;
CC       Name=3;
CC         IsoId=Q01543-3; Sequence=VSP_045276;
CC       Name=4;
CC         IsoId=Q01543-4; Sequence=VSP_046943;
CC   -!- DISEASE: Ewing sarcoma (ES) [MIM:612219]: A highly malignant,
CC       metastatic, primitive small round cell tumor of bone and soft tissue
CC       that affects children and adolescents. It belongs to the Ewing sarcoma
CC       family of tumors, a group of morphologically heterogeneous neoplasms
CC       that share the same cytogenetic features. They are considered neural
CC       tumors derived from cells of the neural crest. Ewing sarcoma represents
CC       the less differentiated form of the tumors.
CC       {ECO:0000269|PubMed:1522903, ECO:0000269|PubMed:1765382}. Note=The gene
CC       represented in this entry is involved in disease pathogenesis. A
CC       chromosomal aberration involving FLI1 is found in patients with Erwing
CC       sarcoma. Translocation t(11;22)(q24;q12) with EWSR1.
CC       {ECO:0000269|PubMed:1522903, ECO:0000269|PubMed:1765382}.
CC   -!- DISEASE: Bleeding disorder, platelet-type 21 (BDPLT21) [MIM:617443]: A
CC       disorder characterized by increased bleeding tendency due to platelet
CC       dysfunction. Clinical features include epistaxis, hematomas, bleeding
CC       after tooth extraction, and menorrhagia. BDPLT21 patients may have mild
CC       to moderate thrombocytopenia. {ECO:0000269|PubMed:24100448,
CC       ECO:0000269|PubMed:26316623, ECO:0000269|PubMed:28255014}. Note=The
CC       disease is caused by mutations affecting the gene represented in this
CC       entry.
CC   -!- MISCELLANEOUS: Located on a fragment of chromosome 11 flanked on the
CC       centromeric side by the acute lymphoblastic leukemia-associated
CC       t(4;11)(q21;q23) translocation breakpoint and on the telomeric side by
CC       the Ewing- and neuroepithelioma-associated t(11;22) (q24;q12)
CC       breakpoint.
CC   -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/FLI1ID79ch11q24.html";
DR   EMBL; X67001; CAA47399.1; -; mRNA.
DR   EMBL; M98833; AAA35812.2; -; mRNA.
DR   EMBL; S45205; AAB23637.1; -; mRNA.
DR   EMBL; M93255; AAA58479.1; -; mRNA.
DR   EMBL; M93255; AAA58480.1; -; mRNA.
DR   EMBL; AY029368; AAK50443.1; -; mRNA.
DR   EMBL; AK294279; BAG57565.1; -; mRNA.
DR   EMBL; AK300153; BAG61938.1; -; mRNA.
DR   EMBL; AK313370; BAG36169.1; -; mRNA.
DR   EMBL; AP001122; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471065; EAW67715.1; -; Genomic_DNA.
DR   EMBL; CH471065; EAW67718.1; -; Genomic_DNA.
DR   EMBL; BC001670; AAH01670.1; -; mRNA.
DR   EMBL; BC010115; AAH10115.1; -; mRNA.
DR   EMBL; Y17293; CAA76731.1; -; Genomic_DNA.
DR   EMBL; D38408; BAA07463.1; ALT_TERM; Genomic_DNA.
DR   CCDS; CCDS44768.1; -. [Q01543-1]
DR   CCDS; CCDS53725.1; -. [Q01543-3]
DR   CCDS; CCDS59230.1; -. [Q01543-4]
DR   CCDS; CCDS59231.1; -. [Q01543-2]
DR   PIR; I37565; I37565.
DR   PIR; S29844; S29844.
DR   RefSeq; NP_001161153.1; NM_001167681.2. [Q01543-3]
DR   RefSeq; NP_001257939.1; NM_001271010.1. [Q01543-2]
DR   RefSeq; NP_001257941.1; NM_001271012.1. [Q01543-4]
DR   RefSeq; NP_002008.2; NM_002017.4. [Q01543-1]
DR   PDB; 1FLI; NMR; -; A=276-373.
DR   PDB; 1X66; NMR; -; A=114-198.
DR   PDB; 2YTU; NMR; -; A=100-220.
DR   PDB; 5E8G; X-ray; 2.70 A; A/B/C/D=276-399.
DR   PDB; 5E8I; X-ray; 3.45 A; A/D/G/J=276-399.
DR   PDB; 5JVT; X-ray; 3.10 A; A/D/G=276-375.
DR   PDBsum; 1FLI; -.
DR   PDBsum; 1X66; -.
DR   PDBsum; 2YTU; -.
DR   PDBsum; 5E8G; -.
DR   PDBsum; 5E8I; -.
DR   PDBsum; 5JVT; -.
DR   BMRB; Q01543; -.
DR   SMR; Q01543; -.
DR   BioGRID; 108602; 37.
DR   CORUM; Q01543; -.
DR   IntAct; Q01543; 7.
DR   MINT; Q01543; -.
DR   STRING; 9606.ENSP00000433488; -.
DR   GlyGen; Q01543; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; Q01543; -.
DR   MetOSite; Q01543; -.
DR   PhosphoSitePlus; Q01543; -.
DR   BioMuta; FLI1; -.
DR   DMDM; 399496; -.
DR   EPD; Q01543; -.
DR   jPOST; Q01543; -.
DR   MassIVE; Q01543; -.
DR   MaxQB; Q01543; -.
DR   PaxDb; Q01543; -.
DR   PeptideAtlas; Q01543; -.
DR   PRIDE; Q01543; -.
DR   ProteomicsDB; 32288; -.
DR   ProteomicsDB; 4083; -.
DR   ProteomicsDB; 57969; -. [Q01543-1]
DR   ProteomicsDB; 57970; -. [Q01543-2]
DR   Antibodypedia; 9350; 656 antibodies.
DR   DNASU; 2313; -.
DR   Ensembl; ENST00000281428; ENSP00000281428; ENSG00000151702. [Q01543-2]
DR   Ensembl; ENST00000344954; ENSP00000339627; ENSG00000151702. [Q01543-4]
DR   Ensembl; ENST00000527786; ENSP00000433488; ENSG00000151702. [Q01543-1]
DR   Ensembl; ENST00000534087; ENSP00000432950; ENSG00000151702. [Q01543-3]
DR   GeneID; 2313; -.
DR   KEGG; hsa:2313; -.
DR   UCSC; uc009zci.4; human. [Q01543-1]
DR   CTD; 2313; -.
DR   DisGeNET; 2313; -.
DR   EuPathDB; HostDB:ENSG00000151702.16; -.
DR   GeneCards; FLI1; -.
DR   HGNC; HGNC:3749; FLI1.
DR   HPA; ENSG00000151702; Tissue enhanced (lymphoid).
DR   MalaCards; FLI1; -.
DR   MIM; 193067; gene.
DR   MIM; 612219; phenotype.
DR   MIM; 617443; phenotype.
DR   neXtProt; NX_Q01543; -.
DR   OpenTargets; ENSG00000151702; -.
DR   Orphanet; 370334; Extraskeletal Ewing sarcoma.
DR   Orphanet; 248340; Isolated delta-storage pool disease.
DR   Orphanet; 2308; Jacobsen syndrome.
DR   Orphanet; 851; Paris-Trousseau thrombocytopenia.
DR   Orphanet; 370348; Peripheral primitive neuroectodermal tumor.
DR   Orphanet; 319; Skeletal Ewing sarcoma.
DR   PharmGKB; PA28170; -.
DR   eggNOG; KOG3806; Eukaryota.
DR   GeneTree; ENSGT00940000158261; -.
DR   HOGENOM; CLU_933700_0_0_1; -.
DR   InParanoid; Q01543; -.
DR   KO; K09436; -.
DR   OMA; TAFFQNM; -.
DR   PhylomeDB; Q01543; -.
DR   TreeFam; TF350537; -.
DR   PathwayCommons; Q01543; -.
DR   Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis.
DR   SIGNOR; Q01543; -.
DR   BioGRID-ORCS; 2313; 46 hits in 897 CRISPR screens.
DR   ChiTaRS; FLI1; human.
DR   EvolutionaryTrace; Q01543; -.
DR   GeneWiki; FLI1; -.
DR   GenomeRNAi; 2313; -.
DR   Pharos; Q01543; Tbio.
DR   PRO; PR:Q01543; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q01543; protein.
DR   Bgee; ENSG00000151702; Expressed in spleen and 204 other tissues.
DR   ExpressionAtlas; Q01543; baseline and differential.
DR   Genevisible; Q01543; HS.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0042025; C:host cell nucleus; IEA:InterPro.
DR   GO; GO:0016604; C:nuclear body; IDA:HPA.
DR   GO; GO:0000790; C:nuclear chromatin; ISA:NTNU_SB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR   GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc.
DR   GO; GO:0008015; P:blood circulation; IEA:Ensembl.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0007599; P:hemostasis; TAS:ProtInc.
DR   GO; GO:0035855; P:megakaryocyte development; IEA:Ensembl.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd08541; SAM_PNT-FLI-1; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 1.10.150.50; -; 1.
DR   InterPro; IPR000418; Ets_dom.
DR   InterPro; IPR035575; Fli-1.
DR   InterPro; IPR003118; Pointed_dom.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR035573; SAM_PNT-FLI-1.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR11849:SF161; PTHR11849:SF161; 1.
DR   Pfam; PF00178; Ets; 1.
DR   Pfam; PF02198; SAM_PNT; 1.
DR   PRINTS; PR00454; ETSDOMAIN.
DR   SMART; SM00413; ETS; 1.
DR   SMART; SM00251; SAM_PNT; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF47769; SSF47769; 1.
DR   PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR   PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR   PROSITE; PS50061; ETS_DOMAIN_3; 1.
DR   PROSITE; PS51433; PNT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative splicing; Chromosomal rearrangement;
KW   Disease mutation; DNA-binding; Nucleus; Phosphoprotein; Proto-oncogene;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..452
FT                   /note="Friend leukemia integration 1 transcription factor"
FT                   /id="PRO_0000204124"
FT   DOMAIN          112..198
FT                   /note="PNT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00762"
FT   DNA_BIND        281..361
FT                   /note="ETS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT   MOD_RES         39
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P26323"
FT   VAR_SEQ         1..197
FT                   /note="MDGTIKEALSVVSDDQSLFDSAYGAAAHLPKADMTASGSPDYGQPHKINPLP
FT                   PQQEWINQPVRVNVKREYDHMNGSRESPVDCSVSKCSKLVGGGESNPMNYNSYMDEKNG
FT                   PPPPNMTTNERRVIVPADPTLWTQEHVRQWLEWAIKEYSLMEIDTSFFQNMDGKELCKM
FT                   NKEDFLRATTLYNTEVLLSHLSYLRES -> MDPG (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046943"
FT   VAR_SEQ         1..76
FT                   /note="MDGTIKEALSVVSDDQSLFDSAYGAAAHLPKADMTASGSPDYGQPHKINPLP
FT                   PQQEWINQPVRVNVKREYDHMNGS -> MEGGLAGERA (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:1765382,
FT                   ECO:0000303|PubMed:8439553"
FT                   /id="VSP_001478"
FT   VAR_SEQ         1..33
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045276"
FT   VARIANT         324
FT                   /note="R -> W (in BDPLT21; decreased function in positive
FT                   regulation of DNA-templated transcription;
FT                   dbSNP:rs773148506)"
FT                   /evidence="ECO:0000269|PubMed:26316623"
FT                   /id="VAR_078929"
FT   VARIANT         337
FT                   /note="R -> Q (in BDPLT21; loss of function in positive
FT                   regulation of DNA-templated transcription; decreased
FT                   localization to nucleus; no effect on protein abundance;
FT                   dbSNP:rs1064797086)"
FT                   /evidence="ECO:0000269|PubMed:28255014"
FT                   /id="VAR_078930"
FT   VARIANT         337
FT                   /note="R -> W (in BDPLT21; loss of function in positive
FT                   regulation of DNA-templated transcription;
FT                   dbSNP:rs1064797083)"
FT                   /evidence="ECO:0000269|PubMed:24100448"
FT                   /id="VAR_078931"
FT   VARIANT         343
FT                   /note="Y -> C (in BDPLT21; loss of function in positive
FT                   regulation of DNA-templated transcription;
FT                   dbSNP:rs1064797084)"
FT                   /evidence="ECO:0000269|PubMed:24100448"
FT                   /id="VAR_078932"
FT   VARIANT         345
FT                   /note="K -> E (in BDPLT21; loss of function in positive
FT                   regulation of DNA-templated transcription; decreased
FT                   localization to nucleus; no effect on protein abundance;
FT                   dbSNP:rs1064797087)"
FT                   /evidence="ECO:0000269|PubMed:28255014"
FT                   /id="VAR_078933"
FT   CONFLICT        69
FT                   /note="E -> V (in Ref. 5; AAA58479)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        77
FT                   /note="Missing (in Ref. 5; AAA58479)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        130
FT                   /note="P -> A (in Ref. 5; AAA58479/AAA58480)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        133
FT                   /note="W -> V (in Ref. 5; AAA58479/AAA58480)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        294
FT                   /note="S -> N (in Ref. 8; BAG61938)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        323
FT                   /note="E -> Q (in Ref. 4; AAB23637 and 5; AAA58479/
FT                   AAA58480)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        426
FT                   /note="Missing (in Ref. 5; AAA58479/AAA58480)"
FT                   /evidence="ECO:0000305"
FT   STRAND          112..114
FT                   /evidence="ECO:0000244|PDB:2YTU"
FT   STRAND          120..122
FT                   /evidence="ECO:0000244|PDB:1X66"
FT   HELIX           130..132
FT                   /evidence="ECO:0000244|PDB:1X66"
FT   HELIX           137..148
FT                   /evidence="ECO:0000244|PDB:1X66"
FT   HELIX           156..159
FT                   /evidence="ECO:0000244|PDB:1X66"
FT   HELIX           164..169
FT                   /evidence="ECO:0000244|PDB:1X66"
FT   HELIX           172..176
FT                   /evidence="ECO:0000244|PDB:1X66"
FT   HELIX           181..195
FT                   /evidence="ECO:0000244|PDB:1X66"
FT   HELIX           283..291
FT                   /evidence="ECO:0000244|PDB:5E8G"
FT   HELIX           294..296
FT                   /evidence="ECO:0000244|PDB:5E8G"
FT   TURN            297..299
FT                   /evidence="ECO:0000244|PDB:5E8G"
FT   STRAND          300..302
FT                   /evidence="ECO:0000244|PDB:5E8I"
FT   STRAND          308..310
FT                   /evidence="ECO:0000244|PDB:5E8G"
FT   HELIX           314..324
FT                   /evidence="ECO:0000244|PDB:5E8G"
FT   HELIX           332..344
FT                   /evidence="ECO:0000244|PDB:5E8G"
FT   STRAND          347..350
FT                   /evidence="ECO:0000244|PDB:5E8G"
FT   STRAND          352..360
FT                   /evidence="ECO:0000244|PDB:5E8G"
FT   HELIX           362..368
FT                   /evidence="ECO:0000244|PDB:5E8G"
SQ   SEQUENCE   452 AA;  50982 MW;  9C2AAEEAF683F3FA CRC64;
     MDGTIKEALS VVSDDQSLFD SAYGAAAHLP KADMTASGSP DYGQPHKINP LPPQQEWINQ
     PVRVNVKREY DHMNGSRESP VDCSVSKCSK LVGGGESNPM NYNSYMDEKN GPPPPNMTTN
     ERRVIVPADP TLWTQEHVRQ WLEWAIKEYS LMEIDTSFFQ NMDGKELCKM NKEDFLRATT
     LYNTEVLLSH LSYLRESSLL AYNTTSHTDQ SSRLSVKEDP SYDSVRRGAW GNNMNSGLNK
     SPPLGGAQTI SKNTEQRPQP DPYQILGPTS SRLANPGSGQ IQLWQFLLEL LSDSANASCI
     TWEGTNGEFK MTDPDEVARR WGERKSKPNM NYDKLSRALR YYYDKNIMTK VHGKRYAYKF
     DFHGIAQALQ PHPTESSMYK YPSDISYMPS YHAHQQKVNF VPPHPSSMPV TSSSFFGAAS
     QYWTSPTGGI YPNPNVPRHP NTHVPSHLGS YY
//
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